3P0X

Crystal structure of isocitrate lyase from Brucella melitensis, bound to magnesium isocitrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004451	molecular_function	isocitrate lyase activity
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004451	molecular_function	isocitrate lyase activity
B	0016829	molecular_function	lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004451	molecular_function	isocitrate lyase activity
C	0016829	molecular_function	lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004451	molecular_function	isocitrate lyase activity
D	0016829	molecular_function	lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 440

Chain	Residue
A	ALA92
A	HOH562
B	ARG116
B	HOH530
B	HOH666

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 445

Chain	Residue
A	HOH475
A	CYS275
A	ASP276
A	LYS304
A	LEU305

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT A 450

Chain	Residue
A	SER84
A	GLY85
A	TRP86
A	ASP147
A	CYS185
A	GLY186
A	HIS187
A	ARG222
A	GLU281
A	ASN309
A	SER311
A	SER313
A	THR343
A	LEU344
A	MG430
A	HOH585
A	HOH586

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 430

Chain	Residue
A	ASP147
A	ICT450
A	HOH584
A	HOH585
A	HOH586

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 445

Chain	Residue
B	ILE19
B	ASP276
B	LYS304
B	LEU305
B	HOH516

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ICT B 450

Chain	Residue
B	TYR82
B	SER84
B	GLY85
B	TRP86
B	ASP147
B	CYS185
B	GLY186
B	HIS187
B	ARG222
B	GLU281
B	ASN309
B	SER311
B	SER313
B	THR343
B	MG430
B	HOH486
B	HOH535
B	HOH536

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 430

Chain	Residue
B	ASP147
B	ICT450
B	HOH486
B	HOH535
B	HOH536

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 445

Chain	Residue
C	ILE19
C	CYS275
C	ASP276
C	LYS304
C	LEU305
C	HOH556

---

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ICT C 450

Chain	Residue
C	SER84
C	GLY85
C	TRP86
C	ASP147
C	CYS185
C	GLY186
C	HIS187
C	ARG222
C	GLU281
C	ASN309
C	SER311
C	SER313
C	THR343
C	MG430
C	HOH517
C	HOH570

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 430

Chain	Residue
C	ASP147
C	ICT450
C	HOH517
C	HOH518
C	HOH570

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 440

Chain	Residue
C	ARG116
C	HOH612
C	HOH664
D	ARG116
D	HOH484

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 445

Chain	Residue
D	ASP276
D	LYS304
D	LEU305
D	HOH555

---

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ICT D 450

Chain	Residue
D	TRP86
D	ASP147
D	CYS185
D	GLY186
D	HIS187
D	ARG222
D	GLU281
D	ASN309
D	SER311
D	SER313
D	THR343
D	LEU344
D	MG430
D	HOH551
D	HOH553
D	TYR82
D	SER84
D	GLY85

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 430

Chain	Residue
D	ASP147
D	ICT450
D	HOH485
D	HOH551
D	HOH553

---

Functional Information from PROSITE/UniProt

site_id	PS00161
Number of Residues	6
Details	ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL

Chain	Residue	Details
A	LYS183-LEU188

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